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Conserved domains on  [gi|74211152|dbj|BAE37658|]
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unnamed protein product [Mus musculus]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 44-183 1.13e-84

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member PRK05692:

Pssm-ID: 473867  Cd Length: 287  Bit Score: 253.27  E-value: 1.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152   44 LPEYVKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQYPGVRYPVLTP 123
Cdd:PRK05692   1 LPKRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGIQRRPGVTYAALTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  124 NLQGFQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:PRK05692  81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYV 140
 
Name Accession Description Interval E-value
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 44-183 1.13e-84

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 253.27  E-value: 1.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152   44 LPEYVKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQYPGVRYPVLTP 123
Cdd:PRK05692   1 LPKRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGIQRRPGVTYAALTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  124 NLQGFQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:PRK05692  81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYV 140
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 50-183 2.23e-84

3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163676  Cd Length: 274  Bit Score: 252.31  E-value: 2.23e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  50 IVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQYPGVRYPVLTPNLQGFQ 129
Cdd:cd07938   1 IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74211152 130 HAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:cd07938  81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYV 134
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 48-173 7.09e-20

HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.


Pssm-ID: 459902 [Multi-domain]  Cd Length: 264  Bit Score: 85.47  E-value: 7.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152    48 VKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVtsfvssrWVPQMA-DHAEVMRGIRQYPGVR--YPVLTPN 124
Cdd:pfam00682   2 VAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEV-------GFPAASeDDFEVVRAIAKVIPHAriLVLCRAR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74211152   125 LQGFQHAVA----AGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSAR 173
Cdd:pfam00682  75 EHDIKAAVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAAR 127
 
Name Accession Description Interval E-value
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 44-183 1.13e-84

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 253.27  E-value: 1.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152   44 LPEYVKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQYPGVRYPVLTP 123
Cdd:PRK05692   1 LPKRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGIQRRPGVTYAALTP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  124 NLQGFQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:PRK05692  81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYV 140
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 50-183 2.23e-84

3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163676  Cd Length: 274  Bit Score: 252.31  E-value: 2.23e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  50 IVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQYPGVRYPVLTPNLQGFQ 129
Cdd:cd07938   1 IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74211152 130 HAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:cd07938  81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYV 134
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
 26-183 9.28e-82

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 248.17  E-value: 9.28e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152   26 DSVAGALDAAQEASQLP-GLPEYVKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHA 104
Cdd:PLN02746  24 SSSSNEVGVAHMHNKLLkGLPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWVPQLADAK 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74211152  105 EVMRGIRQYPGVRYPVLTPNLQGFQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:PLN02746 104 DVMAAVRNLEGARFPVLTPNLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYV 182
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 51-183 4.60e-48

DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163674 [Multi-domain]  Cd Length: 265  Bit Score: 159.16  E-value: 4.60e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  51 VEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMRGIRQY-PGVRYPVLTPN-LQGF 128
Cdd:cd03174   1 TDTTLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASPKAVPQMEDDWEVLRAIRKLvPNVKLQALVRNrEKGI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74211152 129 QHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSARHMDIPVRGYL 183
Cdd:cd03174  81 ERALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAAKEAGLEVEGSL 135
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 48-173 7.09e-20

HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.


Pssm-ID: 459902 [Multi-domain]  Cd Length: 264  Bit Score: 85.47  E-value: 7.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152    48 VKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVtsfvssrWVPQMA-DHAEVMRGIRQYPGVR--YPVLTPN 124
Cdd:pfam00682   2 VAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEV-------GFPAASeDDFEVVRAIAKVIPHAriLVLCRAR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74211152   125 LQGFQHAVA----AGATEIAVFGAASESFSKKNINCSIEESMGRFQEVISSAR 173
Cdd:pfam00682  75 EHDIKAAVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAAR 127
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
 48-180 2.56e-04

Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163685  Cd Length: 262  Bit Score: 41.16  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152  48 VKIVEVGPRDGLQNEKVIVPTDIKIELINQLSQTGLSVIEVTSFVSSrwvPQMADHAEVMRGIrqypGVRYPVLTP---N 124
Cdd:cd07948   1 FKIIDSTLREGEQFANAFFDTEDKIEIAKALDAFGVDYIELTSPAAS---PQSRADCEAIAKL----GLKAKILTHircH 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74211152 125 LQGFQHAVAAGATEIAVFGAASE---SFSK-KNINCSIEESMgrfqEVISSARHMDIPVR 180
Cdd:cd07948  74 MDDARIAVETGVDGVDLVFGTSPflrEASHgKSITEIIESAV----EVIEFVKSKGIEVR 129
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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